MFTE_MYCTU
ID MFTE_MYCTU Reviewed; 251 AA.
AC P9WP59; L0T678; P95041; Q7D9E8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Mycofactocin precursor peptide peptidase;
DE EC=3.4.14.- {ECO:0000250|UniProtKB:A0PM51};
GN Name=mftE {ECO:0000303|PubMed:21223593}; OrderedLocusNames=Rv0695;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP POSSIBLE FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21223593; DOI=10.1186/1471-2164-12-21;
RA Haft D.H.;
RT "Bioinformatic evidence for a widely distributed, ribosomally produced
RT electron carrier precursor, its maturation proteins, and its
RT nicotinoprotein redox partners.";
RL BMC Genomics 12:21-21(2011).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Peptidase involved in the biosynthesis of the enzyme cofactor
CC mycofactocin (MFT). Catalyzes cleavage of the MftC-modified MftA
CC peptide to liberate its final two residues, which consist of a cross-
CC linked valine-decarboxylated tyrosine dipeptide (named 3-amino-5-[(4-
CC hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one or ADHP).
CC {ECO:0000250|UniProtKB:A0PM51}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-
CC hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide +
CC H2O = 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-
CC 2-one + [mycofactocin precursor peptide]-C-terminal glycine;
CC Xref=Rhea:RHEA:65504, Rhea:RHEA-COMP:16818, Rhea:RHEA-COMP:16819,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:83148, ChEBI:CHEBI:150863,
CC ChEBI:CHEBI:156518; Evidence={ECO:0000250|UniProtKB:A0PM51};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:A0PM51};
CC Note=MftE appears to bind one Fe(2+) and one Zn(2+) ion per subunit.
CC Fe(2+) seems to be catalytically active while Zn(2+) could play an
CC auxiliary role. {ECO:0000250|UniProtKB:A0PM51};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A0PM51};
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:A0PM51}.
CC -!- SIMILARITY: Belongs to the creatininase superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP43439.1; -; Genomic_DNA.
DR PIR; B70641; B70641.
DR RefSeq; NP_215209.1; NC_000962.3.
DR RefSeq; WP_003403497.1; NZ_NVQJ01000007.1.
DR AlphaFoldDB; P9WP59; -.
DR SMR; P9WP59; -.
DR STRING; 83332.Rv0695; -.
DR PaxDb; P9WP59; -.
DR DNASU; 888314; -.
DR GeneID; 45424659; -.
DR GeneID; 888314; -.
DR KEGG; mtu:Rv0695; -.
DR TubercuList; Rv0695; -.
DR eggNOG; COG1402; Bacteria.
DR OMA; PCFLWSG; -.
DR PhylomeDB; P9WP59; -.
DR BRENDA; 3.4.14.14; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10310; -; 1.
DR InterPro; IPR024087; Creatininase-like_sf.
DR InterPro; IPR003785; Creatininase/forma_Hydrolase.
DR InterPro; IPR023871; MftE.
DR PANTHER; PTHR35005; PTHR35005; 1.
DR Pfam; PF02633; Creatininase; 1.
DR SUPFAM; SSF102215; SSF102215; 1.
DR TIGRFAMs; TIGR03964; mycofact_creat; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Iron; Metal-binding; Protease; Reference proteome; Zinc.
FT CHAIN 1..251
FT /note="Mycofactocin precursor peptide peptidase"
FT /id="PRO_0000415279"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 128
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P83772"
FT BINDING 167
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P83772"
SQ SEQUENCE 251 AA; 26580 MW; 6C0882C57D15EAF0 CRC64;
MNSSYHRRVP VVGELGSATS SQLPSTSPSI VIPLGSTEQH GPHLPLDTDT RIATAVARTV
TARLHAEDLP IAQEEWLMAP AIAYGASGEH QRFAGTISIG TEALTMLLVE YGRSAACWAR
RLVFVNGHGG NVGALTRAVG LLRAEGRDAG WCPCTCPGGD PHAGHTETSV LLHLSPADVR
TERWRAGNRA PLPVLLPSMR RGGVAAVSET GVLGDPTTAT AAEGRRIFAA MVDDCVRRVA
RWMPQPDGML T
